Erythrocyte membrane phosphatidylcholine and Rh (D) antigen cryolatency.
The extent of binding of anti-D antibody to intact RH (D) positive human erythrocytes at -2.5 degrees was approximately one-third that at 3- degrees. An Arrhenius plot of the temperature dependence of antibody binding showed a clear and reproducible discontinuity at approximately 6-8 degrees. Phospholipase A2 digestion of the intact erythrocytes resulted in a diminution of exclusively phosphatidylcholine (PC) from the membrane, and an approximately parallel loss of Rh antigen activity at 37 degrees to about 50% of the original. An Arrhenius plot showed no change in the temperature dependence below 6-8 degrees but significant diminution above that point suggesting that the outer membrane PC is involved in Rh (D) antigen activity manifested above that temperature.
D003080:Cold Temperature; D004910:Erythrocyte Membrane / Q000276:immunology*; D004912:Erythrocytes / Q000276:immunology*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D010713:Phosphatidylcholines / Q000097:blood / Q000276:immunology*; D010741:Phospholipases A / Q000494:pharmacology; D054467:Phospholipases A2; D012204:Rh-Hr Blood-Group System / Q000276:immunology*; D013205:Staphylococcal Protein A / Q000276:immunology; D013816:Thermodynamics
D010713:Phosphatidylcholines; D012204:Rh-Hr Blood-Group System; D013205:Staphylococcal Protein A; D010741:Phospholipases A; D054467:Phospholipases A2